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- W1567663765 abstract "Abstract 1. 1. The effect of dilution and of pH on the precipitation of nucleohistones and proteolytic enzymes from a solution of calf-thymus chromatin in 1 M NaCl has been studied. 2. 2. The histone-splitting neutral protease (pH optimum 7.8) was precipitated by decreasing salt concentration at neutral pH. The enzyme was extracted from nucleoprotein at low pH values. The protease is less strongly bound to DNA than is the bulk of histones; its precipitation profile is similar to that of lysine-rich histone. The neutral protease, extracted with HCl, is considerably more stable at low pH than the enzyme associated with the precipitated nucleoprotein. It is tentatively concluded that the neutral protease is a normal constituent of calf-thymus chromatin. 3. 3. The acid extract of calf-thymus chromatin was fractionated by means of gel filtration on Sephadex G-100. The neutral protease emerged after the protein peak; the approximate mol. wt. of the enzyme is 24 000. 4. 4. The acid protease (pH optimum 4.4) is not precipitated with reconstituted nucleohistones by decreasing the salt concentration. Its activity is rapidly lost at low pH values." @default.
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- W1567663765 date "1967-09-01" @default.
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- W1567663765 title "Protein catabolism in thymus nuclei" @default.
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- W1567663765 doi "https://doi.org/10.1016/0005-2795(67)90097-9" @default.
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